ID A0A1M7TVN4_9RHOB Unreviewed; 639 AA.
AC A0A1M7TVN4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000256|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_01458};
GN Name=ftsH {ECO:0000256|HAMAP-Rule:MF_01458};
GN ORFNames=SAMN05216200_110106 {ECO:0000313|EMBL:SHN74787.1};
OS Oceanicella actignis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Oceanicella.
OX NCBI_TaxID=1189325 {ECO:0000313|EMBL:SHN74787.1, ECO:0000313|Proteomes:UP000184066};
RN [1] {ECO:0000313|EMBL:SHN74787.1, ECO:0000313|Proteomes:UP000184066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10808 {ECO:0000313|EMBL:SHN74787.1,
RC ECO:0000313|Proteomes:UP000184066};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for
CC both cytoplasmic and membrane proteins. Plays a role in the quality
CC control of integral membrane proteins. {ECO:0000256|HAMAP-
CC Rule:MF_01458}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01458};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01458};
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01458};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01458}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044, ECO:0000256|HAMAP-
CC Rule:MF_01458}.
CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC {ECO:0000256|HAMAP-Rule:MF_01458}.
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DR EMBL; FRDL01000010; SHN74787.1; -; Genomic_DNA.
DR RefSeq; WP_072748174.1; NZ_VNHJ01000002.1.
DR AlphaFoldDB; A0A1M7TVN4; -.
DR STRING; 1189325.SAMN04488119_101526; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000184066; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.720.210; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 1.
DR HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF06480; FtsH_ext; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01458}; Cell cycle {ECO:0000313|EMBL:SHN74787.1};
KW Cell division {ECO:0000313|EMBL:SHN74787.1};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01458};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01458};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01458};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW Rule:MF_01458};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01458};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01458};
KW Reference proteome {ECO:0000313|Proteomes:UP000184066};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01458};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01458}; Zinc {ECO:0000256|HAMAP-Rule:MF_01458}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT DOMAIN 186..325
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 592..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 417
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 194..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 494
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ SEQUENCE 639 AA; 69162 MW; A904E179F92C6348 CRC64;
MGNAKNLAFW AVVILLLVAL FSVFQDGGAS RQGARITFSD FLESVENNQV ASVVIDGERI
AGRLTSGQQF QTVQPRNADI LDDLRAHGVE IMVEPQESSG LLSTLGFWLP MLILIGVWIF
FLNRMQGGGR GGAMGFGKSR AKLLTERTGK VTFDDVAGID EAKEELEEIV EFLRNPQKYS
RLGGKIPKGA LLVGPPGTGK TLLARAIAGE AGVPFFTISG SDFVEMFVGV GASRVRDMFE
QAKKNAPCIV FIDEIDAVGR HRGAGYGGGN DEREQTLNQL LVEMDGFEAN EGVILIAATN
RPDVLDPALL RPGRFDRQVT VPNPDVGGRE KILHVHARKV PLAPNVDLKV IARGTPGFSG
ADLANLVNEA ALTAARLGKR LVTMEDFETA KDKIMMGAER RSMVMTEDEK RLTAYHEAGH
AIVGLNVPQH DPIHKATIIP RGRALGLVLS LPERDHLSVS KTKYESKIAM AMGGKVAEEL
VFGPENVTSG AASDIQQVTR IARAMVTQFG MSERLGNIDY ANEQQSFLGA YQAPAHISPE
TQEIIDEEVR RIVDQGYETA KRILTEKRED LERLAQGLLE YETLTGDEIH KVLRGEPLDR
SDDGGAPPAP EGSAPGVVSI PKAGKRPRDD GGMAPQPQG
//
